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Database: UniProt
Entry: U2L2X7_9FIRM
LinkDB: U2L2X7_9FIRM
Original site: U2L2X7_9FIRM 
ID   U2L2X7_9FIRM            Unreviewed;       331 AA.
AC   U2L2X7;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   SubName: Full=Electron transfer flavoprotein FAD-binding domain protein {ECO:0000313|EMBL:ERJ83789.1};
GN   ORFNames=HMPREF1987_00785 {ECO:0000313|EMBL:ERJ83789.1};
OS   Peptostreptococcaceae bacterium oral taxon 113 str. W5053.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Peptostreptococcaceae.
OX   NCBI_TaxID=1321784 {ECO:0000313|EMBL:ERJ83789.1, ECO:0000313|Proteomes:UP000016618};
RN   [1] {ECO:0000313|EMBL:ERJ83789.1, ECO:0000313|Proteomes:UP000016618}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=W5053 {ECO:0000313|EMBL:ERJ83789.1,
RC   ECO:0000313|Proteomes:UP000016618};
RA   Weinstock G., Sodergren E., Wylie T., Fulton L., Fulton R., Fronick C.,
RA   O'Laughlin M., Godfrey J., Miner T., Herter B., Appelbaum E., Cordes M.,
RA   Lek S., Wollam A., Pepin K.H., Palsikar V.B., Mitreva M., Wilson R.K.;
RL   Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|PIRSR:PIRSR000089-1};
CC       Note=Binds 1 FAD per dimer. {ECO:0000256|PIRSR:PIRSR000089-1};
CC   -!- SIMILARITY: Belongs to the ETF alpha-subunit/FixB family.
CC       {ECO:0000256|ARBA:ARBA00005817}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ERJ83789.1}.
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DR   EMBL; AWVB01000038; ERJ83789.1; -; Genomic_DNA.
DR   AlphaFoldDB; U2L2X7; -.
DR   STRING; 1321784.HMPREF1987_00785; -.
DR   PATRIC; fig|1321784.3.peg.737; -.
DR   eggNOG; COG2025; Bacteria.
DR   HOGENOM; CLU_034178_0_1_9; -.
DR   OrthoDB; 9770286at2; -.
DR   Proteomes; UP000016618; Unassembled WGS sequence.
DR   GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   CDD; cd01715; ETF_alpha; 1.
DR   Gene3D; 3.40.50.620; HUPs; 1.
DR   Gene3D; 3.40.50.1220; TPP-binding domain; 1.
DR   InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR   InterPro; IPR014730; ETF_a/b_N.
DR   InterPro; IPR001308; ETF_a/FixB.
DR   InterPro; IPR033947; ETF_alpha_N.
DR   InterPro; IPR014731; ETF_asu_C.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   PANTHER; PTHR43153; ELECTRON TRANSFER FLAVOPROTEIN ALPHA; 1.
DR   PANTHER; PTHR43153:SF1; ELECTRON TRANSFER FLAVOPROTEIN SUBUNIT ALPHA, MITOCHONDRIAL; 1.
DR   Pfam; PF01012; ETF; 1.
DR   Pfam; PF00766; ETF_alpha; 1.
DR   PIRSF; PIRSF000089; Electra_flavoP_a; 1.
DR   SMART; SM00893; ETF; 1.
DR   SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 1.
DR   SUPFAM; SSF52467; DHS-like NAD/FAD-binding domain; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|PIRSR:PIRSR000089-1};
KW   Flavoprotein {ECO:0000256|PIRSR:PIRSR000089-1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016618}.
FT   DOMAIN          6..189
FT                   /note="Electron transfer flavoprotein alpha/beta-subunit N-
FT                   terminal"
FT                   /evidence="ECO:0000259|SMART:SM00893"
FT   BINDING         259..263
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000089-1"
FT   BINDING         276..283
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000089-1"
FT   BINDING         297
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000089-1"
SQ   SEQUENCE   331 AA;  36657 MW;  459368A969CBDA44 CRC64;
     MDHKNIFVLM EINQGQLFPV SLELINIGKQ LACQRKQELV AILIGKDIQK IAEEILYYGV
     DRILLIEGEE YENYSTDAYT YALENVLTKH QPLACLLPAT PNGRDLGGRI SARMNLGLVA
     GCTDIYFQED TNTINWVRPT FNGKLYSAIQ TTTHPQIGTI DMGVFRTAKK VTHPNGKIEE
     EKISFQTENI RTKFLKFLPN DKPTKKTPLE QADIVVCAGM GVGSEENIQL VKDLADALGA
     TFGVTKLLVD ARWAPYDIQI GATGVTVSPK LYIGVGVSGA GQHWHGIKKA KTIIAINKDK
     DAPIMHEAHY SIVGDLFEIL PPLIEKIKKQ A
//
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